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Information on EC 3.4.24.70 - oligopeptidase A
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EC Tree
3.4.24.70 oligopeptidase ASpecify your search results
Word Map
- 3.4.24.70
-
prolyl
- typhimurium
-
dipeptidyl
- carboxypeptidase
- neuropeptides
- endopeptidases
-
oxyanion
- subtilisin
- octapeptide
-
post-proline
-
thimet
- neurolysin
- z-pro-prolinal
-
bell-shaped
-
product-like
-
scissile
-
3.4.24.15
-
arrhenius
- metallopeptidase
- bradykinin
The enzyme appears in viruses and cellular organisms
Reaction Schemes
hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
Synonyms
oligopeptidase a, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
68000-M Signalpeptide hydrolase
-
-
-
-
oligopeptidase A
OpdA
prlC
additional information
-
the enzyme belongs to the M3 peptidase family with four conserved Tyr residues on a flexible loop in close proximity to the catalytic site
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
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-
-
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hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
the Tyr607 residue is involved in the recognition of the substrate with a key role in catalysis, it plays an important role in the enzyme-substrate interaction and in the hydrolytic activity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
148266-37-9
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394250-11-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-casein-derived peptides + H2O
?
-
alpha-casein is not cleaved by OpdA, but by proteases HslUV, ClpAP, or Lon, the peptide products are then cleaved by OpdA, overview
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-
?
bacteriophage P22 gp7 protein
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
Benzyloxycarbonyl-Ala-Ala + Leu 4-nitroanilide
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly + Gly-Pro-Ala
o-aminobenzoyl-NKPRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
best substrate for OpdA
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-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
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-
-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
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-
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
-
-
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
-
directly or indirectly involved in post-translational processing, required for normal growth of phage P22
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-
?
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
Benzyloxycarbonyl-Ala-Ala + Leu 4-nitroanilide
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-
-
?
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
Benzyloxycarbonyl-Ala-Ala + Leu 4-nitroanilide
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-
-
?
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly + Gly-Pro-Ala
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-
-
?
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly + Gly-Pro-Ala
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-
-
?
o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
-
-
-
?
o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
-
-
-
?
Prolipoprotein signal peptide + H2O
?
-
further degrades partially degraded portions of signal peptide yielded by protease IV
-
-
?
Prolipoprotein signal peptide + H2O
?
-
in vitro studies suggest oligopeptidase A may be involved in degradation of signal peptides
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-
?
Prolipoprotein signal peptide + H2O
?
-
in vitro studies suggest oligopeptidase A may be involved in degradation of signal peptides
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-
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
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-
smallest fragment: tripeptide
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
-
proposed cleavage sites
peptide fragments identified
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
-
methionine-labelled
peptide fragments identified
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
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smallest fragment: tripeptide
?
additional information
?
-
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benzyloxycarbonyl-Gly-Gly-Gly-Gly or benzyloxycarbonyl-Gly-Gly-Gly-Gly-Gly
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?
additional information
?
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substrates are N-blocked peptides with at least 4 amino acid residues or unblocked pentapeptides, no substrates are signal peptide still attached to the mature protein
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-
?
additional information
?
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no cleavage of Abz-GFPPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
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?
additional information
?
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substrate specificities and cleavage sites of OpdA mutants, overview
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-
?
additional information
?
-
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no cleavage of Abz-GFPPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
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?
additional information
?
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the enzyme digests proteins to short peptides that are subsequently hydrolyzed to smaller fragments and free amino acids, protein degradation is an essential quality control and regulatory function
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-
?
additional information
?
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the enzyme cleaves peptides generated by the activity of the three primary ATP-dependent proteases Lon, HslUV, and ClpAP from Escherichia coli, overview
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-
?
additional information
?
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benzyloxycarbonyl-Gly-Gly-Gly-Gly or benzyloxycarbonyl-Gly-Gly-Gly-Gly-Gly
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-
?
additional information
?
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benzyloxycarbonyl-Gly-Gly-Gly-Gly or benzyloxycarbonyl-Gly-Gly-Gly-Gly-Gly
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-
?
additional information
?
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hydrolyzes N-blocked peptides containing at least four amino acids but is unable to hydrolyze unblocked peptides with fewer than five amino acids, Gly or Ala on either side of the scissile bond is permissive for hydrolysis
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme digests proteins to short peptides that are subsequently hydrolyzed to smaller fragments and free amino acids, protein degradation is an essential quality control and regulatory function
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
-
-
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
-
directly or indirectly involved in post-translational processing, required for normal growth of phage P22
-
-
?
Prolipoprotein signal peptide + H2O
?
-
further degrades partially degraded portions of signal peptide yielded by protease IV
-
-
?
Prolipoprotein signal peptide + H2O
?
-
in vitro studies suggest oligopeptidase A may be involved in degradation of signal peptides
-
-
?
Prolipoprotein signal peptide + H2O
?
-
in vitro studies suggest oligopeptidase A may be involved in degradation of signal peptides
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
Mn2+
Zn2+
additional information
Mn2+
-
activation, to a lesser extent than Co2+, 0.1 mM
additional information
OpdA is a metalloproteinase
additional information
-
putative Zn2+-binding site
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenylmethylsulfonyl fluoride
PMSF, 80% inhibition at 1 mM
salicylate
interacts with the isozyme and inhibits its peptidase activity to various degrees both in vitro and in plant extracts; interacts with the isozyme and inhibits its peptidase activity to various degrees both in vitro and in plant extracts. Specific isozyme TOP2salicylate interaction may be dependent on plant-specific modifications of isozyme TOP2
salicylic acid
inhibits the peptidase activity of isozyme TOP1 and to a lesser extent isozyme TOP2; inhibits the peptidase activity of isozyme TOP1 and to a lesser extent isozyme TOP2
trans-epoxysuccinyl L-leucylamido-(4-guanidino)butane
E-64, 25% inhibition at 0.01 mM
additional information
-
not inhibited by 0.2 mM leupeptin, 0.1 mM PMSF, 0.1 mM E-64, 0.001 mM Z-pro-prolinal and 0.02 mM captopril
-
additional information
-
not inhibited by captopril
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Memory Disorders
Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site.
Memory Disorders
Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase.
Neuroinflammatory Diseases
Prolyl Oligopeptidase: A Rising Star on the Stage of Neuroinflammation Research.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0662
-
with o-aminobenzoyl-GFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.0833
-
with o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.0858
-
with o-aminobenzoyl-RPPGFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.1129
-
with o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.289
-
with o-aminobenzoyl-NKPRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
